MX2007012570A - Terapia de anticuerpo anti-egfr basada en un numero de copia creciente del gen egfr en tejidos de tumor. - Google Patents
Terapia de anticuerpo anti-egfr basada en un numero de copia creciente del gen egfr en tejidos de tumor.Info
- Publication number
- MX2007012570A MX2007012570A MX2007012570A MX2007012570A MX2007012570A MX 2007012570 A MX2007012570 A MX 2007012570A MX 2007012570 A MX2007012570 A MX 2007012570A MX 2007012570 A MX2007012570 A MX 2007012570A MX 2007012570 A MX2007012570 A MX 2007012570A
- Authority
- MX
- Mexico
- Prior art keywords
- egfr
- cancer
- copy number
- gene
- tumor
- Prior art date
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EP05008156 | 2005-04-14 | ||
PCT/EP2006/003358 WO2006108627A1 (en) | 2005-04-14 | 2006-04-12 | Anti-egfr antibody therapy based on an increased copy number of the egfr gene in tumor tissues |
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MX2007012570A MX2007012570A (es) | 2005-04-14 | 2006-04-12 | Terapia de anticuerpo anti-egfr basada en un numero de copia creciente del gen egfr en tejidos de tumor. |
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US (1) | US20090269344A1 (zh) |
EP (1) | EP1869208A1 (zh) |
JP (1) | JP2008535508A (zh) |
KR (1) | KR20080003422A (zh) |
CN (1) | CN101155932A (zh) |
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BR (1) | BRPI0610440A2 (zh) |
CA (1) | CA2604300A1 (zh) |
MX (1) | MX2007012570A (zh) |
RU (1) | RU2007141067A (zh) |
WO (1) | WO2006108627A1 (zh) |
ZA (1) | ZA200709780B (zh) |
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EP1869220A2 (en) * | 2005-04-01 | 2007-12-26 | Amgen, Inc. | Epidermal growth factor receptor gene copy number |
US7908091B2 (en) | 2006-03-17 | 2011-03-15 | Prometheus Laboratories Inc. | Methods of predicting and monitoring tyrosine kinase inhibitor therapy |
NZ578943A (en) | 2007-03-01 | 2012-09-28 | Symphogen As | Recombinant anti-epidermal growth factor receptor antibody compositions |
CL2008000717A1 (es) | 2007-03-13 | 2008-09-22 | Amgen Inc | Metodo para pronosticar si un paciente sera no respondedor al tratamiento con un agente de union especifica a un polipeptido de egfr que comprende determinar la presencia o ausencia de una mutacion de k-ras en un tumor del paciente. |
EP2118322A2 (en) * | 2007-03-13 | 2009-11-18 | Amgen Inc. | K-ras and b-raf mutations and anti-egfr antibody therapy |
JP5719298B2 (ja) | 2008-08-29 | 2015-05-13 | シムフォゲン・アクティーゼルスカブSymphogen A/S | 組換え抗上皮増殖因子受容体抗体組成物 |
EP3216874A1 (en) | 2008-09-05 | 2017-09-13 | TOMA Biosciences, Inc. | Methods for stratifying and annotating cancer drug treatment options |
KR101918004B1 (ko) * | 2009-10-26 | 2018-11-13 | 애보트 모레큘러 인크. | 비-소세포 폐암의 예후를 측정하기 위한 진단 방법 |
US8609354B2 (en) * | 2010-03-04 | 2013-12-17 | Olli CARPEN | Method for selecting patients for treatment with an EGFR inhibitor |
WO2011107664A1 (en) | 2010-03-04 | 2011-09-09 | Hospital District Of Southwest Finland | Method for selecting patients for treatment with an egfr inhibitor |
US20120045433A1 (en) * | 2010-08-17 | 2012-02-23 | Kapil Dhingra | Combination therapy |
US8709419B2 (en) | 2010-08-17 | 2014-04-29 | Hoffmann-La Roche, Inc. | Combination therapy |
EP3572528A1 (en) | 2010-09-24 | 2019-11-27 | The Board of Trustees of the Leland Stanford Junior University | Direct capture, amplification and sequencing of target dna using immobilized primers |
DE102010060964A1 (de) * | 2010-12-02 | 2012-06-06 | Universitätsklinikum Hamburg-Eppendorf | Verfahren zur Prädikation der therapeutischen Wirksamkeit von EGFR-Inhibitoren |
US9295669B2 (en) | 2010-12-14 | 2016-03-29 | Hoffman La-Roche Inc. | Combination therapy for proliferative disorders |
CN102153648B (zh) * | 2011-01-27 | 2012-07-04 | 中国人民解放军军事医学科学院生物工程研究所 | 一种抗egfr人源化抗体l4-h3及其编码基因与应用 |
CN103619881B (zh) | 2011-04-07 | 2017-07-28 | 安姆根有限公司 | 新的egfr结合蛋白 |
CN104145027A (zh) * | 2011-12-12 | 2014-11-12 | 塞雷公司 | 用于室温原位检测生物样品中的目标核酸的方法和试剂盒 |
AU2015205755C1 (en) | 2014-01-10 | 2020-08-13 | Birdie Biopharmaceuticals Inc. | Compounds and compositions for immunotherapy |
KR102462743B1 (ko) | 2014-07-09 | 2022-11-02 | 버디 바이오파마슈티칼즈, 인크. | 종양 치료용 항-pd-l1 조합 |
JP6782698B2 (ja) * | 2014-12-12 | 2020-11-11 | セルキュイティー インコーポレイテッド | がん患者を診断および処置するためのerbbシグナル伝達経路活性の測定方法 |
CN115252792A (zh) * | 2016-01-07 | 2022-11-01 | 博笛生物科技有限公司 | 用于治疗肿瘤的抗-egfr组合 |
CN115554406A (zh) | 2016-01-07 | 2023-01-03 | 博笛生物科技有限公司 | 用于治疗肿瘤的抗-cd20组合 |
CN108794467A (zh) | 2017-04-27 | 2018-11-13 | 博笛生物科技有限公司 | 2-氨基-喹啉衍生物 |
EP3641771A4 (en) | 2017-06-23 | 2020-12-16 | Birdie Biopharmaceuticals, Inc. | PHARMACEUTICAL COMPOSITIONS |
WO2019109086A1 (en) * | 2017-12-01 | 2019-06-06 | Illumina, Inc. | Methods and systems for determining somatic mutation clonality |
EP3591666A1 (en) * | 2018-07-04 | 2020-01-08 | Dassault Systèmes | Simulating evolution of a tumor |
CN112430646A (zh) * | 2020-12-11 | 2021-03-02 | 南京求臻基因科技有限公司 | 一种基于数字pcr平台的egfr基因扩增的检测方法 |
CN112646893A (zh) * | 2021-01-08 | 2021-04-13 | 北京泛生子基因科技有限公司 | 一种egfr基因拷贝数检测试剂盒及检测方法 |
Family Cites Families (3)
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ES2331646T3 (es) * | 2000-05-19 | 2010-01-12 | Genentech, Inc. | Ensayo para la deteccion de genes para mejorar la probabilidad de una respuesta eficaz a una terapia contra el cancer basada en antagonistas de erbb. |
AU2004248140A1 (en) * | 2003-05-30 | 2004-12-23 | Cedars-Sinai Medical Center | Gene expression markers for response to EGFR inhibitor drugs |
EP1869220A2 (en) * | 2005-04-01 | 2007-12-26 | Amgen, Inc. | Epidermal growth factor receptor gene copy number |
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- 2006-04-12 US US11/911,380 patent/US20090269344A1/en not_active Abandoned
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WO2006108627A1 (en) | 2006-10-19 |
CN101155932A (zh) | 2008-04-02 |
ZA200709780B (en) | 2008-11-26 |
US20090269344A1 (en) | 2009-10-29 |
KR20080003422A (ko) | 2008-01-07 |
JP2008535508A (ja) | 2008-09-04 |
BRPI0610440A2 (pt) | 2010-06-22 |
WO2006108627A9 (en) | 2007-10-11 |
AU2006233675A1 (en) | 2006-10-19 |
CA2604300A1 (en) | 2006-10-19 |
EP1869208A1 (en) | 2007-12-26 |
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